FMO DATABASE

FMODB ID: N9G2Q

Calculation Name: 2ABL-A-Xray372

Preferred Name: Tyrosine-protein kinase ABL

Target Type: SINGLE PROTEIN

Ligand Name:

ligand 3-letter code:

PDB ID: 2ABL

Chain ID: A

ChEMBL ID: CHEMBL1862

UniProt ID: P00519

Base Structure: X-ray

Registration Date: 2023-09-19

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptH
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	163
LigandCharge
Software	ABINIT-MP - Open Ver. 1 Rev. 22 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-1524568.118815
FMO2-HF: Nuclear repulsion	1461634.501738
FMO2-HF: Total energy	-62933.617078
FMO2-MP2: Total energy	-63120.023374

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:75:MET)

Summations of interaction energy for fragment #1(A:75:MET)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
-5.871	-2.159	0.323	-2.246	-1.788	0

Interaction energy analysis for fragmet #1(A:75:MET)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.022 / q_NPA : -0.009

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].
3	A	77	PRO	0	-0.008	-0.026	2.686	-6.506	-2.770	0.324	-2.237	-1.823
4	A	78	SER	0	0.033	0.025	4.865	-0.344	-0.368	-0.001	-0.009	0.035
5	A	79	GLU	-1	-0.875	-0.954	6.182	-0.309	-0.309	0.000	0.000	0.000
6	A	80	ASN	0	-0.039	-0.010	8.735	0.181	0.181	0.000	0.000	0.000
7	A	81	ASP	-1	-0.863	-0.933	8.830	-0.626	-0.626	0.000	0.000	0.000
8	A	82	PRO	0	-0.022	-0.035	10.889	0.035	0.035	0.000	0.000	0.000
9	A	83	ASN	0	-0.018	0.003	12.498	0.092	0.092	0.000	0.000	0.000
10	A	84	LEU	0	-0.049	-0.002	8.967	0.022	0.022	0.000	0.000	0.000
11	A	85	PHE	0	0.038	0.011	11.889	0.061	0.061	0.000	0.000	0.000
12	A	86	VAL	0	-0.065	-0.047	13.712	-0.034	-0.034	0.000	0.000	0.000
13	A	87	ALA	0	0.046	0.033	15.938	0.018	0.018	0.000	0.000	0.000
14	A	88	LEU	0	-0.052	-0.048	18.601	-0.004	-0.004	0.000	0.000	0.000
15	A	89	TYR	0	-0.063	-0.039	21.948	0.005	0.005	0.000	0.000	0.000
16	A	90	ASP	-1	-0.807	-0.904	21.359	0.018	0.018	0.000	0.000	0.000
17	A	91	PHE	0	-0.037	-0.007	21.459	-0.004	-0.004	0.000	0.000	0.000
18	A	92	VAL	0	-0.026	-0.026	21.787	0.013	0.013	0.000	0.000	0.000
19	A	93	ALA	0	0.003	-0.005	21.944	-0.008	-0.008	0.000	0.000	0.000
20	A	94	SER	0	-0.015	-0.004	23.904	0.004	0.004	0.000	0.000	0.000
21	A	95	GLY	0	0.020	-0.002	25.842	0.000	0.000	0.000	0.000	0.000
22	A	96	ASP	-1	-0.838	-0.895	21.129	0.201	0.201	0.000	0.000	0.000
23	A	97	ASN	0	-0.090	-0.051	22.205	-0.022	-0.022	0.000	0.000	0.000
24	A	98	THR	0	-0.016	0.000	22.431	-0.012	-0.012	0.000	0.000	0.000
25	A	99	LEU	0	-0.006	0.010	14.987	0.017	0.017	0.000	0.000	0.000
26	A	100	SER	0	0.017	0.005	19.115	-0.029	-0.029	0.000	0.000	0.000
27	A	101	ILE	0	-0.038	-0.005	16.064	0.015	0.015	0.000	0.000	0.000
28	A	102	THR	0	0.008	0.016	16.791	0.000	0.000	0.000	0.000	0.000
29	A	103	LYS	1	0.925	0.947	17.374	0.027	0.027	0.000	0.000	0.000
30	A	104	GLY	0	-0.037	-0.012	16.996	0.011	0.011	0.000	0.000	0.000
31	A	105	GLU	-1	-0.910	-0.973	12.343	0.055	0.055	0.000	0.000	0.000
32	A	106	LYS	1	0.867	0.939	10.140	0.304	0.304	0.000	0.000	0.000
33	A	107	LEU	0	0.026	0.014	11.493	0.053	0.053	0.000	0.000	0.000
34	A	108	ARG	1	0.918	0.973	8.930	0.164	0.164	0.000	0.000	0.000
35	A	109	VAL	0	-0.040	-0.026	11.917	0.089	0.089	0.000	0.000	0.000
36	A	110	LEU	0	-0.005	-0.001	13.276	-0.034	-0.034	0.000	0.000	0.000
37	A	111	GLY	0	0.014	0.011	16.748	-0.004	-0.004	0.000	0.000	0.000
38	A	112	TYR	0	0.004	0.013	20.451	0.001	0.001	0.000	0.000	0.000
39	A	113	ASN	0	0.038	0.013	23.403	0.000	0.000	0.000	0.000	0.000
40	A	114	HIS	0	-0.008	-0.022	26.461	-0.007	-0.007	0.000	0.000	0.000
41	A	115	ASN	0	-0.003	0.006	29.797	-0.002	-0.002	0.000	0.000	0.000
42	A	116	GLY	0	0.000	0.003	26.073	-0.005	-0.005	0.000	0.000	0.000
43	A	117	GLU	-1	-0.930	-0.946	25.897	-0.017	-0.017	0.000	0.000	0.000
44	A	118	TRP	0	-0.012	0.002	24.325	0.005	0.005	0.000	0.000	0.000
45	A	119	CYS	0	-0.021	0.004	19.466	-0.012	-0.012	0.000	0.000	0.000
46	A	120	GLU	-1	-0.936	-0.963	18.185	0.079	0.079	0.000	0.000	0.000
47	A	121	ALA	0	0.009	-0.001	15.507	-0.030	-0.030	0.000	0.000	0.000
48	A	122	GLN	0	0.021	-0.012	10.392	0.002	0.002	0.000	0.000	0.000
49	A	123	THR	0	0.044	0.019	10.409	-0.080	-0.080	0.000	0.000	0.000
50	A	124	LYS	1	0.902	0.943	4.802	0.217	0.217	0.000	0.000	0.000
51	A	125	ASN	0	0.011	0.010	8.991	0.191	0.191	0.000	0.000	0.000
52	A	126	GLY	0	0.010	0.014	12.221	-0.001	-0.001	0.000	0.000	0.000
53	A	127	GLN	0	0.020	-0.003	13.304	0.017	0.017	0.000	0.000	0.000
54	A	128	GLY	0	0.021	0.027	15.561	0.007	0.007	0.000	0.000	0.000
55	A	129	TRP	0	-0.039	-0.041	18.641	-0.025	-0.025	0.000	0.000	0.000
56	A	130	VAL	0	0.025	0.024	18.599	0.010	0.010	0.000	0.000	0.000
57	A	131	PRO	0	0.012	0.012	21.678	-0.009	-0.009	0.000	0.000	0.000
58	A	132	SER	0	0.007	-0.032	22.428	-0.006	-0.006	0.000	0.000	0.000
59	A	133	ASN	0	-0.006	-0.014	23.321	-0.007	-0.007	0.000	0.000	0.000
60	A	134	TYR	0	0.003	0.004	22.756	0.003	0.003	0.000	0.000	0.000
61	A	135	ILE	0	-0.018	0.004	18.174	-0.003	-0.003	0.000	0.000	0.000
62	A	136	THR	0	-0.024	-0.009	18.901	0.006	0.006	0.000	0.000	0.000
63	A	137	PRO	0	0.032	0.012	17.207	-0.024	-0.024	0.000	0.000	0.000
64	A	138	VAL	0	-0.019	0.011	13.202	0.009	0.009	0.000	0.000	0.000
65	A	139	ASN	0	-0.074	-0.053	12.134	0.048	0.048	0.000	0.000	0.000
66	A	140	SER	0	0.061	0.031	16.051	0.000	0.000	0.000	0.000	0.000
67	A	141	LEU	0	0.023	-0.013	18.192	-0.004	-0.004	0.000	0.000	0.000
68	A	142	GLU	-1	-0.918	-0.973	20.502	-0.105	-0.105	0.000	0.000	0.000
69	A	143	LYS	1	0.896	0.998	16.091	0.296	0.296	0.000	0.000	0.000
70	A	144	HIS	0	-0.004	-0.002	19.457	0.011	0.011	0.000	0.000	0.000
71	A	145	SER	0	-0.002	-0.013	24.235	0.006	0.006	0.000	0.000	0.000
72	A	146	TRP	0	0.063	0.038	22.127	0.007	0.007	0.000	0.000	0.000
73	A	147	TYR	0	-0.120	-0.109	23.760	0.004	0.004	0.000	0.000	0.000
74	A	148	HIS	0	0.005	-0.015	26.286	0.003	0.003	0.000	0.000	0.000
75	A	149	GLY	0	0.079	0.079	26.422	0.003	0.003	0.000	0.000	0.000
76	A	150	PRO	0	-0.019	-0.013	27.402	0.003	0.003	0.000	0.000	0.000
77	A	151	VAL	0	0.037	0.023	30.142	0.003	0.003	0.000	0.000	0.000
78	A	152	SER	0	0.029	0.022	33.348	0.000	0.000	0.000	0.000	0.000
79	A	153	ARG	1	0.935	0.947	36.078	0.035	0.035	0.000	0.000	0.000
80	A	154	ASN	0	0.041	0.002	37.579	-0.001	-0.001	0.000	0.000	0.000
81	A	155	ALA	0	0.040	0.030	37.172	0.000	0.000	0.000	0.000	0.000
82	A	156	ALA	0	0.033	0.011	35.255	-0.001	-0.001	0.000	0.000	0.000
83	A	157	GLU	-1	-0.897	-0.956	36.934	-0.041	-0.041	0.000	0.000	0.000
84	A	158	TYR	0	-0.034	0.010	40.038	0.000	0.000	0.000	0.000	0.000
85	A	159	LEU	0	0.010	0.001	34.776	0.000	0.000	0.000	0.000	0.000
86	A	160	LEU	0	-0.043	0.001	35.696	-0.001	-0.001	0.000	0.000	0.000
87	A	161	SER	0	-0.038	-0.036	39.542	0.002	0.002	0.000	0.000	0.000
88	A	162	SER	0	-0.080	-0.037	42.007	0.002	0.002	0.000	0.000	0.000
89	A	163	GLY	0	0.044	0.017	40.361	-0.003	-0.003	0.000	0.000	0.000
90	A	164	ILE	0	0.004	0.005	38.766	0.003	0.003	0.000	0.000	0.000
91	A	165	ASN	0	0.003	-0.012	40.145	-0.002	-0.002	0.000	0.000	0.000
92	A	166	GLY	0	0.094	0.048	37.002	-0.002	-0.002	0.000	0.000	0.000
93	A	167	SER	0	-0.074	-0.033	35.230	-0.005	-0.005	0.000	0.000	0.000
94	A	168	PHE	0	-0.018	-0.026	28.199	0.003	0.003	0.000	0.000	0.000
95	A	169	LEU	0	0.003	0.019	30.560	-0.002	-0.002	0.000	0.000	0.000
96	A	170	VAL	0	-0.013	-0.009	25.407	0.003	0.003	0.000	0.000	0.000
97	A	171	ARG	1	0.866	0.939	28.368	0.055	0.055	0.000	0.000	0.000
98	A	172	GLU	-1	-0.830	-0.906	24.279	-0.106	-0.106	0.000	0.000	0.000
99	A	173	SER	0	-0.065	-0.041	28.130	0.005	0.005	0.000	0.000	0.000
100	A	174	GLU	-1	-0.891	-0.955	29.429	-0.049	-0.049	0.000	0.000	0.000
101	A	175	SER	0	-0.015	0.005	30.712	-0.001	-0.001	0.000	0.000	0.000
102	A	176	SER	0	0.035	0.012	26.739	-0.004	-0.004	0.000	0.000	0.000
103	A	177	PRO	0	0.089	0.032	23.525	-0.001	-0.001	0.000	0.000	0.000
104	A	178	GLY	0	0.006	0.015	23.446	-0.012	-0.012	0.000	0.000	0.000
105	A	179	GLN	0	-0.045	-0.016	24.394	-0.001	-0.001	0.000	0.000	0.000
106	A	180	ARG	1	1.002	0.994	20.650	0.123	0.123	0.000	0.000	0.000
107	A	181	SER	0	-0.103	-0.054	27.650	0.009	0.009	0.000	0.000	0.000
108	A	182	ILE	0	0.024	0.030	28.390	-0.006	-0.006	0.000	0.000	0.000
109	A	183	SER	0	-0.029	-0.030	31.255	0.006	0.006	0.000	0.000	0.000
110	A	184	LEU	0	0.006	0.000	34.282	-0.004	-0.004	0.000	0.000	0.000
111	A	185	ARG	1	0.950	0.997	36.407	0.049	0.049	0.000	0.000	0.000
112	A	186	TYR	0	-0.034	-0.020	39.680	-0.002	-0.002	0.000	0.000	0.000
113	A	187	GLU	-1	-0.862	-0.939	41.905	-0.038	-0.038	0.000	0.000	0.000
114	A	188	GLY	0	-0.010	0.006	44.815	0.002	0.002	0.000	0.000	0.000
115	A	189	ARG	1	0.907	0.959	44.515	0.035	0.035	0.000	0.000	0.000
116	A	190	VAL	0	0.039	0.017	38.624	-0.002	-0.002	0.000	0.000	0.000
117	A	191	TYR	0	-0.030	-0.004	38.690	0.004	0.004	0.000	0.000	0.000
118	A	192	HIS	0	-0.048	-0.025	35.995	-0.006	-0.006	0.000	0.000	0.000
119	A	193	TYR	0	0.011	0.012	32.844	0.003	0.003	0.000	0.000	0.000
120	A	194	ARG	1	0.896	0.938	31.165	0.041	0.041	0.000	0.000	0.000
121	A	195	ILE	0	0.015	0.025	24.925	0.000	0.000	0.000	0.000	0.000
122	A	196	ASN	0	-0.061	-0.039	27.377	0.001	0.001	0.000	0.000	0.000
123	A	197	THR	0	0.024	0.010	21.537	-0.014	-0.014	0.000	0.000	0.000
124	A	198	ALA	0	-0.062	-0.027	23.468	0.012	0.012	0.000	0.000	0.000
125	A	199	SER	0	0.022	-0.009	22.902	-0.007	-0.007	0.000	0.000	0.000
126	A	200	ASP	-1	-0.843	-0.920	19.468	-0.044	-0.044	0.000	0.000	0.000
127	A	201	GLY	0	0.017	0.008	18.434	-0.007	-0.007	0.000	0.000	0.000
128	A	202	LYS	1	0.857	0.938	19.588	0.093	0.093	0.000	0.000	0.000
129	A	203	LEU	0	0.010	0.016	19.798	0.014	0.014	0.000	0.000	0.000
130	A	204	TYR	0	-0.022	-0.012	22.941	-0.001	-0.001	0.000	0.000	0.000
131	A	205	VAL	0	0.019	0.023	26.375	0.002	0.002	0.000	0.000	0.000
132	A	206	SER	0	0.043	0.003	29.893	0.007	0.007	0.000	0.000	0.000
133	A	207	SER	0	-0.016	-0.009	29.596	-0.004	-0.004	0.000	0.000	0.000
134	A	208	GLU	-1	-0.889	-0.946	29.261	-0.039	-0.039	0.000	0.000	0.000
135	A	209	SER	0	-0.097	-0.057	27.657	-0.004	-0.004	0.000	0.000	0.000
136	A	210	ARG	1	0.895	0.938	23.802	0.048	0.048	0.000	0.000	0.000
137	A	211	PHE	0	0.006	-0.008	21.182	-0.004	-0.004	0.000	0.000	0.000
138	A	212	ASN	0	-0.038	-0.016	14.727	0.023	0.023	0.000	0.000	0.000
139	A	213	THR	0	0.017	0.010	16.078	-0.006	-0.006	0.000	0.000	0.000
140	A	214	LEU	0	0.077	0.014	18.029	0.019	0.019	0.000	0.000	0.000
141	A	215	ALA	0	-0.014	-0.002	19.298	0.015	0.015	0.000	0.000	0.000
142	A	216	GLU	-1	-0.821	-0.925	19.034	-0.179	-0.179	0.000	0.000	0.000
143	A	217	LEU	0	-0.036	0.016	21.654	0.016	0.016	0.000	0.000	0.000
144	A	218	VAL	0	0.002	-0.012	24.178	0.012	0.012	0.000	0.000	0.000
145	A	219	HIS	0	0.007	0.005	22.197	0.006	0.006	0.000	0.000	0.000
146	A	220	HIS	0	-0.012	-0.005	25.665	0.004	0.004	0.000	0.000	0.000
147	A	221	HIS	1	0.815	0.889	27.469	0.090	0.090	0.000	0.000	0.000
148	A	222	SER	0	-0.010	0.014	29.193	0.007	0.007	0.000	0.000	0.000
149	A	223	THR	0	-0.075	-0.044	29.146	0.004	0.004	0.000	0.000	0.000
150	A	224	VAL	0	0.013	0.006	31.460	0.007	0.007	0.000	0.000	0.000
151	A	225	ALA	0	0.016	0.022	32.561	-0.003	-0.003	0.000	0.000	0.000
152	A	226	ASP	-1	-0.828	-0.887	31.535	-0.070	-0.070	0.000	0.000	0.000
153	A	227	GLY	0	0.075	0.034	33.286	-0.003	-0.003	0.000	0.000	0.000
154	A	228	LEU	0	-0.096	-0.036	32.028	0.003	0.003	0.000	0.000	0.000
155	A	229	ILE	0	-0.005	-0.002	35.995	0.001	0.001	0.000	0.000	0.000
156	A	230	THR	0	-0.023	-0.014	37.639	0.002	0.002	0.000	0.000	0.000
157	A	231	THR	0	-0.016	0.009	33.968	0.000	0.000	0.000	0.000	0.000
158	A	232	LEU	0	-0.010	-0.013	29.199	0.003	0.003	0.000	0.000	0.000
159	A	233	HIS	0	0.009	0.009	33.132	0.000	0.000	0.000	0.000	0.000
160	A	234	TYR	0	0.004	-0.003	24.864	-0.006	-0.006	0.000	0.000	0.000
161	A	235	PRO	0	-0.016	-0.013	28.907	0.005	0.005	0.000	0.000	0.000
162	A	236	ALA	0	0.019	0.020	30.481	-0.005	-0.005	0.000	0.000	0.000
163	A	237	PRO	0	-0.013	-0.009	28.851	-0.002	-0.002	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:75:MET)